[Effect of glucose 1-phosphate and inorganic phosphate on binding of muscle phosphorylase b by glycogen].
Using analytical ultracentrifugation, the affinity of rabbit skeletal muscle phosphorylase b for glycogen was shown to increase 11.6-fold in the presence of saturating concentrations of glucose 1-phosphate and to decrease 3.7-fold in the presence of saturating concentrations of inorganic phosphate (20 degrees, 0.05 M glycyl-glycine buffer, pH 6.8, ionic strength 0.3).
D000818:Animals; D005958:Glucosephosphates / Q000494:pharmacology*; D006003:Glycogen / Q000378:metabolism*; D007700:Kinetics; D008433:Mathematics; D009132:Muscles / Q000378:metabolism*; D010710:Phosphates / Q000494:pharmacology*; D010763:Phosphorylase b / Q000378:metabolism*; D006005:Phosphorylases / Q000378:metabolism*; D011485:Protein Binding; D011817:Rabbits
D005958:Glucosephosphates; D010710:Phosphates; D006003:Glycogen; C031590:glucose-1-phosphate; D010763:Phosphorylase b; D006005:Phosphorylases
Vliianie gliukozo-1-fosfata na sviazyvanie myshechnoĭ glikogenfosforilazy b glikogenom.